2KQ3

Solution structure of SNase140

2KQ3 の概要

• エントリーDOI: 10.2210/pdb2kq3/pdb
• NMR情報: BMRB: 16585
• 分子名称: Thermonuclease (1 entity in total)
• 機能のキーワード: nuclease, hydrolase
• 由来する生物種: Staphylococcus aureus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15914.53

構造登録者

Wang, M.,Feng, Y.,Yao, H.,Wang, J. (登録日: 2009-10-26, 公開日: 2010-05-26, 最終更新日: 2024-05-15)

主引用文献

Wang, M.,Feng, Y.,Yao, H.,Wang, J.
Importance of the C-Terminal Loop L137-S141 for the Folding and Folding Stability of Staphylococcal Nuclease
Biochemistry, 49:4318-4326, 2010

PubMed Abstract: The role of the C-terminal loop L137-S141 in the folding and folding stability of staphylococcal nuclease (SNase) was investigated by deletion mutation. The C-terminal truncated SNase fragments, SNase137, SNase139, SNase140, and SNase141 containing residues 1-137, 1-139, 1-140, and 1-141, respectively, were adopted in this study. Folding states of these four SNase fragments were analyzed by circular dichroism and fluorescence measurements. The solution structure of SNase140 was determined and compared to those of SNase141 and native SNase using the heteronuclear NMR method. The results showed that folding of the four SNase fragments is correlated with the folding of helix alpha3. With the chain length extending from L137 and I139 to S141, folding of the fragments progressively approached to the tertiary folding of native SNase, and the folding stability was enhanced. These observations revealed that the C-terminal loop L137-S141 has profound effect not only on the folding of helix alpha3 but also on the stabilizing folding of both the alpha- and beta-subdomains of SNase. Analysis indicates that stabilizing folding of the SNase and SNase fragments depends to a large extent on the hydrophobic packing interactions in both the C-terminal local structural region surrounding W140 including the loop L137-S141 and the N-terminal local structural region of the "beta-barrel" hydrophobic core.

PubMed: 20415411
DOI: 10.1021/bi100118k

実験手法

SOLUTION NMR